Alternative RNA splicing generates transcripts encoding a thorax-specific isoform of Drosophila melanogaster myosin heavy chain.

Bernstein, Sanford I.; Hansen, C J; Becker, K D; Wassenberg, D R; Roche, E S; Donady, J J; Emerson, Charles P.

doi:10.1128/mcb.6.7.2511

Cited by 87 publications

(54 citation statements)

References 46 publications

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“…3 A) . This pattern of expression is consistent with the observed time course of larval muscle differentiation and growth (Poulson, 1950 ;Crossley, 1978 ;Bate, 1990) as well as the early developmental expression of the Drosophila MHC gene (Rozek and Davidson, 1983 ;Bernstein et al ., 1986) and the troponin I gene (Barbas et al ., 1991) .…”

Section: A Single Paramyosin Gene Produces Four Mrna Size Classessupporting

confidence: 66%

Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles.

Becker

O'Donnell

Heitz

et al. 1992

The Journal of Cell Biology

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Abstract. In this report we show that Drosophila melanogaster muscles contain the standard form of the thick filament protein paramyosin, as well as a novel paramyosin isoform, which we call miniparamyosin . We have isolated Drosophila paramyosin using previously established methods. This protein is =105 kD and cross-reacts with polyclonal antibodies made against Caenorhabditis elegans or Heliocopris dilloni paramyosin. The Heliocopris antibody also cross-reacts with a

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Section: A Single Paramyosin Gene Produces Four Mrna Size Classessupporting

confidence: 66%

Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles.

Becker

O'Donnell

Heitz

et al. 1992

The Journal of Cell Biology

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“…The pattern for Mhc 1~ larvae is identical to that of wild type. At the pupal stage, both larval size classes of mRNA accumulate in wild-type organisms, as do two additional transcripts (6.6 and 7.1 kb) that result from inclusion of the 3' penultimate exon and polyadenylation at either of two sites {Bemstein et al 1986;Rozek and Davidson 1986). Note that the smaller-sized pupal-specific mRNA containing the 3' penultimate exon comigrates with the larger sized mRNA lacking that exon.…”

Section: Stage-and Tissue-specific Use Of the Alternative Hingecodingmentioning

confidence: 99%

“…2). At the larval stage, two size classes of transcripts {6.1 and 6.6 kb) accumulate in the wild type; these arise from the use of alternative polyadenylation sites and exclusion of the 3' penultimate exon (Bemstein et al 1986;Rozek and Davidson 1986). Both larval transcript classes hybridize to exon 15b, but neither hybridizes to exon 15a.…”

Section: Stage-and Tissue-specific Use Of the Alternative Hingecodingmentioning

confidence: 99%

Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed.

Collier¹,

Kronert²,

O'Donnell³

et al. 1990

Genes Dev.

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By comparing the structure of wild-type and mutant muscle myosin heavy chain (MHC) genes of Drosophila melanogaster, we have identified the defect in the homozygous-viable, flightless mutant Mhc 10. The mutation is within the 3' splice acceptor of an alternative exon (exon 15a) that encodes the central region of the MHC hinge. The splice acceptor defect prevents the accumulation of mRNAs containing exon 15a, whereas transcripts with a divergent copy of this exon (exon 15b) are unaffected by the mutation. In situ hybridization and Northern blot analysis of wild-type organisms reveals that exon 15b is used in larval MHCs, whereas exons 15a and/or 15b are used in adult tissues. Because Mhc ~~ mutants fail to accumulate transcripts encoding MHC protein with hinge region a, analysis of their muscle-specific reduction in thick filament number serves as a sensitive assay system for determining the pattern of accumulation of MI-ICs with alternative hinge regions. Electron microscopic comparisons of various muscles from wild-type and Mhc ~~ adults reveals that those that contract rapidly or develop high levels of tension utilize only hinge region a, those that contract at moderate rates accumulate MHCs of both types, and those that are slowly contracting have MI-ICs with hinge region b. The presence of alternative hinge-coding exons and their highly tissue-specific usage suggests that this portion of the MHC molecule is important to the isoform-specific properties of MHC that lead to the different physiological and ultrastructural characteristics of various Drosophila muscle types. The absence of other alternative exons in the rod-coding region, aside from those shown previously to encode alternative carboxyl termini, demonstrates that the bulk of the myosin rod is not involved in the generation of isoform-specific properties of the MHC molecule.

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“…However, only one MHC protein isoform is expressed in Drosophila flight muscles (Bernstein et al, 1986) and little is known about MHC isoform composition of flight muscles of any other insects; this raises the question of how insects regulate and vary muscle performance.…”

Section: +mentioning

confidence: 99%

Parasites, proteomics and performance: effects of gregarine gut parasites on dragonfly flight muscle composition and function

Schilder

Marden

2007

Journal of Experimental Biology

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SUMMARY In previous work, we found that dragonflies infected with gregarine gut parasites have reduced muscle power output, loss of lipid oxidation in their flight muscles, and a suite of symptoms similar to mammalian metabolic syndrome. Here, we test the hypothesis that changes in muscle protein composition underlie the observed changes in contractile performance. We found that gregarine infection was associated with a 10-fold average reduction in abundance of a ∼155 kDa fragment of muscle myosin heavy chain (MHC;∼206 kDa intact size). Insect MHC gene sequences contain evolutionarily conserved amino acid motifs predicted for calpain cleavage, and we found that calpain digestion of purified dragonfly MHC produced a peptide of ∼155 kDa. Thus, gut parasites in dragonflies are associated with what appears to be a reduction in proteolytic degradation of MHC. MHC155 abundance showed a strong negative relationship to muscle power output in healthy dragonflies but either no relationship or a weakly positive relationship in infected dragonflies. Troponin T (TnT) protein isoform profiles were not significantly different between healthy and infected dragonflies but whereas TnT isoform profile was correlated with power output in healthy dragonflies, there was no such correlation in infected dragonflies. Multivariate analyses of power output based on MHC155 abundance and a principal component of TnT protein isoform abundances explained 98% of the variation in muscle power output in healthy dragonflies but only 29% when data from healthy and infected dragonflies were pooled. These results indicate that important, yet largely unexplored, functional relationships exist between (pathways regulating)myofibrillar protein expression and (post-translational) protein processing. Moreover, infection by protozoan parasites of the midgut is associated with changes in muscle protein composition (i.e. across body compartments) that,either alone or in combination with other unmeasured changes, alter muscle contractile performance.

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Alternative RNA splicing generates transcripts encoding a thorax-specific isoform of Drosophila melanogaster myosin heavy chain.

Cited by 87 publications

References 46 publications

Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles.

Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles.

Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed.

Parasites, proteomics and performance: effects of gregarine gut parasites on dragonfly flight muscle composition and function

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